Header list of 1y7x.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN, PROTEIN BINDING 10-DEC-04 1Y7X
TITLE SOLUTION STRUCTURE OF A TWO-REPEAT FRAGMENT OF MAJOR VAULT PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR VAULT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAINS 3-4 OF MVP REPEATS (RESIDUES 113-221);
COMPND 5 SYNONYM: MVP, LUNG RESISTANCE-RELATED PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MVP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS STRUCTURAL REPEATS, BETA-SHEET MODULES, STRUCTURAL PROTEIN, PROTEIN
KEYWDS 2 BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.KOZLOV,O.VAVELYUK,O.MINAILIUC,D.BANVILLE,K.GEHRING,I.EKIEL
REVDAT 4 02-MAR-22 1Y7X 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1Y7X 1 VERSN
REVDAT 2 21-MAR-06 1Y7X 1 JRNL
REVDAT 1 20-DEC-05 1Y7X 0
JRNL AUTH G.KOZLOV,O.VAVELYUK,O.MINAILIUC,D.BANVILLE,K.GEHRING,I.EKIEL
JRNL TITL SOLUTION STRUCTURE OF A TWO-REPEAT FRAGMENT OF MAJOR VAULT
JRNL TITL 2 PROTEIN.
JRNL REF J.MOL.BIOL. V. 356 444 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16373071
JRNL DOI 10.1016/J.JMB.2005.11.064
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, XPLOR-NIH 2.9.2
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1083 RESTRAINTS, 930 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 124 DIHEDRAL ANGLE RESTRAINTS, 29 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1Y7X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031228.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 150MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM MVP U-15N, 20MM BIS-TRIS,
REMARK 210 150MM NACL, 2MM CACL2, 15MM DTT,
REMARK 210 90% H2O, 10% D2O; 1MM MVP, 20MM
REMARK 210 BIS-TRIS, 150MM NACL, 2MM CACL2,
REMARK 210 15MM DTT, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; 2D
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, XEASY 1.3.13, CYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 -RESONANCE AND HOMONUCLEAR TECHNIQUES.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 HIS A 3 178.02 52.91
REMARK 500 1 GLN A 5 -155.72 -112.60
REMARK 500 1 VAL A 7 106.43 -38.78
REMARK 500 1 ALA A 31 75.27 40.79
REMARK 500 1 PRO A 40 23.54 -77.27
REMARK 500 1 THR A 58 63.16 173.61
REMARK 500 1 ILE A 59 -31.98 -171.18
REMARK 500 1 ARG A 61 -153.23 -112.17
REMARK 500 1 LYS A 72 -94.66 -108.32
REMARK 500 1 GLU A 73 29.72 164.39
REMARK 500 1 GLU A 81 101.71 -43.56
REMARK 500 1 ALA A 95 -143.32 -162.46
REMARK 500 1 TYR A 96 104.43 177.17
REMARK 500 1 ALA A 99 -171.56 -65.20
REMARK 500 1 ASP A 106 -166.55 -173.30
REMARK 500 2 SER A 2 172.07 -49.37
REMARK 500 2 MET A 4 -164.91 -125.90
REMARK 500 2 ASN A 10 64.48 60.71
REMARK 500 2 LYS A 28 120.44 172.59
REMARK 500 2 THR A 58 38.97 -179.49
REMARK 500 2 ILE A 59 -74.31 -159.90
REMARK 500 2 ARG A 61 -166.37 -113.36
REMARK 500 2 GLN A 62 -70.82 -75.61
REMARK 500 2 CYS A 74 -16.01 75.05
REMARK 500 2 ALA A 95 -175.23 -176.42
REMARK 500 2 ALA A 99 -178.94 51.87
REMARK 500 2 VAL A 100 -63.93 -97.21
REMARK 500 2 ASP A 106 -178.80 -177.95
REMARK 500 2 ALA A 110 45.29 26.06
REMARK 500 3 SER A 2 -69.95 65.23
REMARK 500 3 VAL A 6 -133.30 -74.80
REMARK 500 3 ASN A 10 27.29 -163.46
REMARK 500 3 ASP A 27 -156.46 -64.27
REMARK 500 3 LYS A 28 131.14 174.92
REMARK 500 3 PRO A 45 74.58 -66.22
REMARK 500 3 VAL A 52 -60.78 -96.54
REMARK 500 3 THR A 58 45.31 -179.51
REMARK 500 3 ILE A 59 -53.24 -162.48
REMARK 500 3 GLN A 62 -70.25 -58.85
REMARK 500 3 GLU A 73 103.49 -56.59
REMARK 500 3 CYS A 74 -33.02 179.27
REMARK 500 3 LYS A 80 -70.35 -114.89
REMARK 500 3 GLU A 81 119.59 171.36
REMARK 500 3 ALA A 95 154.79 178.67
REMARK 500 3 ALA A 99 174.91 68.29
REMARK 500 3 PHE A 101 53.43 -109.45
REMARK 500 3 VAL A 111 -122.70 44.16
REMARK 500 3 ILE A 112 -70.86 -107.13
REMARK 500 4 SER A 2 -91.89 49.55
REMARK 500 4 HIS A 3 -93.03 49.57
REMARK 500
REMARK 500 THIS ENTRY HAS 362 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 46 0.31 SIDE CHAIN
REMARK 500 1 ARG A 61 0.32 SIDE CHAIN
REMARK 500 1 ARG A 69 0.32 SIDE CHAIN
REMARK 500 1 ARG A 71 0.26 SIDE CHAIN
REMARK 500 1 ARG A 77 0.28 SIDE CHAIN
REMARK 500 1 ARG A 82 0.29 SIDE CHAIN
REMARK 500 2 ARG A 46 0.31 SIDE CHAIN
REMARK 500 2 ARG A 61 0.31 SIDE CHAIN
REMARK 500 2 ARG A 67 0.27 SIDE CHAIN
REMARK 500 2 ARG A 69 0.31 SIDE CHAIN
REMARK 500 2 ARG A 71 0.31 SIDE CHAIN
REMARK 500 2 ARG A 77 0.20 SIDE CHAIN
REMARK 500 2 ARG A 82 0.31 SIDE CHAIN
REMARK 500 3 ARG A 46 0.14 SIDE CHAIN
REMARK 500 3 ARG A 61 0.21 SIDE CHAIN
REMARK 500 3 ARG A 67 0.29 SIDE CHAIN
REMARK 500 3 ARG A 69 0.30 SIDE CHAIN
REMARK 500 3 ARG A 71 0.31 SIDE CHAIN
REMARK 500 3 ARG A 77 0.24 SIDE CHAIN
REMARK 500 3 ARG A 82 0.32 SIDE CHAIN
REMARK 500 4 ARG A 46 0.23 SIDE CHAIN
REMARK 500 4 ARG A 61 0.13 SIDE CHAIN
REMARK 500 4 ARG A 67 0.32 SIDE CHAIN
REMARK 500 4 ARG A 71 0.32 SIDE CHAIN
REMARK 500 4 ARG A 77 0.24 SIDE CHAIN
REMARK 500 4 ARG A 82 0.20 SIDE CHAIN
REMARK 500 5 ARG A 46 0.22 SIDE CHAIN
REMARK 500 5 ARG A 67 0.32 SIDE CHAIN
REMARK 500 5 ARG A 69 0.28 SIDE CHAIN
REMARK 500 5 ARG A 71 0.08 SIDE CHAIN
REMARK 500 5 ARG A 77 0.20 SIDE CHAIN
REMARK 500 5 ARG A 82 0.24 SIDE CHAIN
REMARK 500 6 ARG A 46 0.12 SIDE CHAIN
REMARK 500 6 ARG A 61 0.25 SIDE CHAIN
REMARK 500 6 ARG A 67 0.27 SIDE CHAIN
REMARK 500 6 ARG A 69 0.24 SIDE CHAIN
REMARK 500 6 ARG A 71 0.27 SIDE CHAIN
REMARK 500 6 ARG A 77 0.32 SIDE CHAIN
REMARK 500 6 ARG A 82 0.08 SIDE CHAIN
REMARK 500 7 ARG A 46 0.32 SIDE CHAIN
REMARK 500 7 ARG A 61 0.20 SIDE CHAIN
REMARK 500 7 ARG A 67 0.20 SIDE CHAIN
REMARK 500 7 ARG A 69 0.32 SIDE CHAIN
REMARK 500 7 ARG A 71 0.31 SIDE CHAIN
REMARK 500 7 ARG A 77 0.30 SIDE CHAIN
REMARK 500 7 ARG A 82 0.27 SIDE CHAIN
REMARK 500 8 ARG A 46 0.19 SIDE CHAIN
REMARK 500 8 ARG A 61 0.19 SIDE CHAIN
REMARK 500 8 ARG A 67 0.24 SIDE CHAIN
REMARK 500 8 ARG A 69 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 132 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Y7X A 5 113 UNP Q14764 MVP_HUMAN 113 221
SEQADV 1Y7X GLY A 1 UNP Q14764 CLONING ARTIFACT
SEQADV 1Y7X SER A 2 UNP Q14764 CLONING ARTIFACT
SEQADV 1Y7X HIS A 3 UNP Q14764 CLONING ARTIFACT
SEQADV 1Y7X MET A 4 UNP Q14764 CLONING ARTIFACT
SEQRES 1 A 113 GLY SER HIS MET GLN VAL VAL LEU PRO ASN THR ALA LEU
SEQRES 2 A 113 HIS LEU LYS ALA LEU LEU ASP PHE GLU ASP LYS ASP GLY
SEQRES 3 A 113 ASP LYS VAL VAL ALA GLY ASP GLU TRP LEU PHE GLU GLY
SEQRES 4 A 113 PRO GLY THR TYR ILE PRO ARG LYS GLU VAL GLU VAL VAL
SEQRES 5 A 113 GLU ILE ILE GLN ALA THR ILE ILE ARG GLN ASN GLN ALA
SEQRES 6 A 113 LEU ARG LEU ARG ALA ARG LYS GLU CYS TRP ASP ARG ASP
SEQRES 7 A 113 GLY LYS GLU ARG VAL THR GLY GLU GLU TRP LEU VAL THR
SEQRES 8 A 113 THR VAL GLY ALA TYR LEU PRO ALA VAL PHE GLU GLU VAL
SEQRES 9 A 113 LEU ASP LEU VAL ASP ALA VAL ILE LEU
HELIX 1 1 PRO A 40 TYR A 43 5 4
SHEET 1 A 3 ASP A 33 GLU A 38 0
SHEET 2 A 3 ALA A 12 ALA A 17 -1 N LEU A 15 O TRP A 35
SHEET 3 A 3 VAL A 49 ILE A 55 -1 O VAL A 52 N HIS A 14
SHEET 1 B 2 ASP A 20 PHE A 21 0
SHEET 2 B 2 VAL A 29 VAL A 30 -1 O VAL A 29 N PHE A 21
SHEET 1 C 3 GLU A 87 VAL A 90 0
SHEET 2 C 3 GLN A 64 ALA A 70 -1 N LEU A 66 O VAL A 90
SHEET 3 C 3 GLU A 102 ASP A 109 -1 O GLU A 103 N ARG A 69
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes